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Merck
CN

P9498

Monoclonal Anti-PIAS-x antibody produced in mouse

clone PIASX-116, purified immunoglobulin, buffered aqueous solution

别名:

Anti-Protein Inhibitor of Activator STAT

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
PIASX-116, monoclonal
Application:
ARR, ELISA (i), ICC, WB
Citations:
4
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biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

PIASX-116, monoclonal

form

buffered aqueous solution

mol wt

antigen ~75 kDa

species reactivity

human

technique(s)

immunocytochemistry: suitable, indirect ELISA: suitable, microarray: suitable, western blot: 1-2 μg/mL using proteasome fraction II of HeLa cells

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PIAS2(9063)

General description

Monoclonal Anti-PIAS-x (mouse IgG1isotype) is derived from the PIASX-116 hybridoma produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice. Protein inhibitor of activated STAT 2 (PIAS2/PIAS-x), a small ubiquitin-like modifier (SUMO) E3 ligase contains a zinc binding motif and a highly acidic region. This gene is located on human chromosome 18q21.1.

Immunogen

peptide corresponding to amino acids 26-40 of human PIAS-x.

Application

Monoclonal Anti-PIAS-x antibody produced in mouse may be used in:
  • enzyme-linked immunosorbent assay (ELISA)
  • immunocytochemistry
  • immunoblotting

Biochem/physiol Actions

Monoclonal Anti-PIAS-x recognizes human PIAS-x.
Protein inhibitor of activated STAT2 (PIAS2) plays a key role in SUMO modification (SUMOylation) of several host and viral proteins. PIAS-x acts as a transcriptional co-repressor of STAT4. It may participate in controlling the chromatin structure. Upregulation or suppression of this gene can control the stability of the hepatitis C virus (HCV) core, NS3 and NS5A proteins. Hence PIAS-x is considered as the restriction factor for HCV replication.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

Preparation Note

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in “frost-free” freezers is also not recom-mended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Ulf R Klein et al.
Molecular biology of the cell, 20(1), 410-418 (2008-10-24)
The ubiquitin-like SUMO system controls cellular key functions, and several lines of evidence point to a critical role of SUMO for mitotic progression. However, in mammalian cells mitotic substrates of sumoylation and the regulatory components involved are not well defined.
Protein inhibitor of activated STAT2 restricts HCV replication by modulating viral proteins degradation
Guo J, et al.
Viruses, 9(10), 285-285 (2017)
Search for inherited susceptibility to radiation-associated meningioma by genomewide SNP linkage disequilibrium mapping
Hosking FJ, et al.
British Journal of Cancer, 104(6), 1049-1054 (2011)
W Rozek et al.
Polish journal of veterinary sciences, 16(4), 663-669 (2013-01-01)
Changes in the level of cellular proteins in cells inoculated with equine influenza virus H7N7 and H3N8 were studied with microarray technique. H3N8 induced pro-apoptotic proteins while H7N7 induced both pro- as well as anti-apoptotic factors. The higher level of

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